Domain

Isopropylmalate dehydrogenase-like domain (IPR024084)

Short name: IsoPropMal-DH-like_dom

Overlapping homologous superfamilies

None.

Domain relationships

None.

Description

The isocitrate and isopropylmalate dehydrogenases family includes isocitrate dehydrogenase (IDH), 3-isopropylmalate dehydrogenase (IMDH) and tartrate dehydrogenase.

IDH is an important enzyme of carbohydrate metabolism which catalyses the oxidative decarboxylation of isocitrate into alpha-ketoglutarate [PMID: 2682654, PMID: 1939242]. IDH is either dependent on NAD+ (EC:1.1.1.41) or on NADP+ (EC:1.1.1.42). In eukaryotes there are at least three isozymes of IDH: two are located in the mitochondrial matrix (one NAD+-dependent, the other NADP+-dependent), while the third one (also NADP+-dependent) is cytoplasmic. In Escherichia coli, the activity of a NADP+-dependent form of the enzyme is controlled by the phosphorylation of a serine residue; the phosphorylated form of IDH is completely inactivated.

IMDH (EC:1.1.1.85) catalyses the third step in the biosynthesis of leucine in bacteria and fungi, the oxidative decarboxylation of 3-isopropylmalate into 2-oxo-4-methylvalerate [PMID: 1748999, PMID: 7773180].

Tartrate dehydrogenase (EC:1.1.1.93) shows strong homology to prokaryotic isopropylmalate dehydrogenases and, to a lesser extent, isocitrate dehydrogenase [PMID: 8053675]. It catalyses the reduction of tartrate to oxaloglycolate [PMID: 8053675].

This entry represents a structural domain found in all types of isocitrate dehydrogenase, and in isopropylmalate dehydrogenase and tartrate dehydrogenase. The crystal structure of Escherichia coli isopropylmalate dehydrogenase has been described [PMID: 9086278].

GO terms

Biological Process

GO:0055114 oxidation-reduction process

Molecular Function

GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
SMART
Pfam